Fibrillin-1 and −2 contain heparin-binding sites important for matrix deposition and that support cell attachment

Ritty, Timothy M.; Broekelmann, Thomas J.; Werneck, Cláudio C.; Mecham, Robert P.

doi:10.1042/bj20030649

Cited by 73 publications

(89 citation statements)

References 26 publications

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“…Fibrillin-1 isolated from human fibroblasts appears as linear fibrils with a beaded periodicity (Sakai et al, 1991). Fibrillins have ArgGly-Asp (RGD) sequences that interact with integrins (Pfaff et al, 1996;Sakamoto et al, 1996;Bax et al, 2003) and heparin-binding domains that interact with cell surface heparan sulfate proteoglycans (Tiedemann et al, 2001;Ritty et al, 2003), suggesting that fibrillins directly signal cells through these receptors. Furthermore, in vivo assembly of fibrillin may require cell-surface receptors in a similar manner to fibronectin (Wu et al, 1995).…”

Section: Fibrillinsmentioning

confidence: 99%

New insights into elastic fiber assembly

Wagenseil

Mecham

2007

Birth Defects Research Pt C

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344

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Elastic fibers provide recoil to tissues that undergo repeated stretch, such as the large arteries and lung. These large extracellular matrix (ECM) structures contain numerous components, and our understanding of elastic fiber assembly is changing as we learn more about the various molecules associated with the assembly process. The main components of elastic fibers are elastin and microfibrils. Elastin makes up the bulk of the mature fiber and is encoded by a single gene. Microfibrils consist mainly of fibrillin, but also contain or associate with proteins such as microfibril associated glycoproteins (MAGPs), fibulins, and EMILIN-1. Microfibrils were thought to facilitate alignment of elastin monomers prior to cross-linking by lysyl oxidase (LOX). We now know that their role, as well as the overall assembly process, is more complex. Elastic fiber formation involves elaborate spatial and temporal regulation of all of the involved proteins and is difficult to recapitulate in adult tissues. This report summarizes the known interactions between elastin and the microfibrillar proteins and their role in elastic fiber assembly based on in vitro studies and evidence from knockout mice. We also propose a model of elastic fiber assembly based on the current data that incorporates interactions between elastin, LOXs, fibulins and the microfibril, as well as the pivotal role played by cells in structuring the final functional fiber. Birth Defects Research (Part C) 81:229-240,

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Section: Fibrillinsmentioning

confidence: 99%

New insights into elastic fiber assembly

Wagenseil

Mecham

2007

Birth Defects Research Pt C

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344

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“…XF and the fibrillins also share homology in their carboxy-terminal sequences, which do not correspond to any recognizable modular protein motif. However, this region includes both a conserved furin proprotein convertase processing site at which profibrillins are matured by proteolytic processing, as well as a region that exhibits cell binding activity (Lonnqvist et al, 1998;Ritty et al, 2003). XF also exhibited eight N-linked glycosylation sites of which six are conserved in at least two of the three human fibrillins.…”

Section: Identification Of Cdna's Encoding Xenopus Fibrillin (Xf)mentioning

confidence: 99%

“…One role is to multimerize into microfibrils, which can perform biomechanical roles in the body (Robinson and Godfrey, 2000). Fibrillins 1 and 2 have been shown to be ligands for both integrin and proteoglycan cell surface receptors (Pfaff et al, 1996;Sakamoto et al, 1996;Ritty et al, 2003;Bax et al, 2003;Cain et al, 2005). These interactions likely mechanically link cells to fibrillin containing matrix (Czirok et al, 2004), and signaling functions through these receptors are possible based on analogy with other matrix molecules such as laminins (Hopker et al, 1999).…”

Section: Roles For Fibrillin In Embryosmentioning

confidence: 99%

Xenopus fibrillin is expressed in the organizer and is the earliest component of matrix at the developing notochord‐somite boundary

Skoglund

Dzamba

Coffman

et al. 2006

Developmental Dynamics

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We identify a Xenopus fibrillin homolog (XF), and show that its earliest developmental expression is in presumptive dorsal mesoderm at gastrulation, and that XF expression is regulated by mesoderm-inducing factors in animal cap assays. XF protein is also first detected in presumptive mesoderm, but is concentrated specifically into extracellular-matrix structures that begin to develop de novo by mid-gastrulation at both of the bilateral presumptive notochord-somite boundaries. Later in embryogenesis, XF protein is localized to the extracellular matrix at tissue boundaries, where it is found surrounding the notochord, the somites, and the neural tube, as well as under the epidermis. This pattern of protein deposition combines to give the appearance of an "embryonic skeleton," suggesting that one role for XF is to serve as a mechanical element in the embryo prior to bone deposition.

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“…10,11 Along with integrin-ligand interactions, another major mode of cell-matrix interaction employs cell-surface heparan-sulphated proteoglycans (HSPGs) such as members of the syndecan or glypican families. 12 Recently, Ritty et al 13 suggested that cell attachment to fibrillins can potentially produce simultaneous signaling from members of these two ECM receptor families: the integrins and the cell-surface HSPGs. Thus, fibrillin may act as a classical adhesion protein with specific interactions with the cellular cytoskeleton involving transmembrane receptors.…”

mentioning

confidence: 99%

“…9 Moreover, given the functional roles of integrins and HSPGs it is already clear that fibrillins play important roles in cell migration, adhesion, signaling, protein-protein interaction and induction of differentiation. 13 As all these procedures are also important during neoplastic transformation and tumor progression, the investigation of fibrillin expression in tumorous conditions seems challenging.…”

mentioning

confidence: 99%

Fibrillin expression and localization in various types of carcinomas of the thyroid gland

et al. 2006

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Fibrillin is an extracellular matrix (ECM) glycoprotein, a main component of microfibrills, suggested to support cell attachment and to impact cell differentiation and migration. The aim of this study was to investigate fibrillin-1 expression in thyroid carcinomas at mRNA and protein level, since ECM proteins are suggested to be of great importance for the metastatic potential of carcinomas. RNA was extracted from 13 thyroid carcinoma cell lines and RT-PCR analysis with gene-specific primers revealed fibrillin-1 mRNA expression in all cell lines, with highest expression in the follicular carcinoma cell line WRO and lowest expression in the two anaplastic cell lines (APO, FRO). Furthermore, we investigated fibrillin-1 expression by immumohistochemistry in a commercially available tissue microarray including 50 thyroid carcinomas as well as in archival tissue from 33 thyroid carcinomas. Fibrillin-1 demonstrated a cytoplasmic location in the neoplastic cells of almost all carcinomas apart from the follicular ones. The most intense staining was observed in papillary carcinomas with some evidence of a slight increased intensity in advanced stages. Our data indicate that fibrillin-1 is strongly expressed by the neoplastic cells of thyroid carcinomas in different degree in the various histologic types and might be implicated in cell-stroma interaction in terms of signaling, attachment and migration.

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Fibrillin-1 and −2 contain heparin-binding sites important for matrix deposition and that support cell attachment

Cited by 73 publications

References 26 publications

New insights into elastic fiber assembly

New insights into elastic fiber assembly

Xenopus fibrillin is expressed in the organizer and is the earliest component of matrix at the developing notochord‐somite boundary

Fibrillin expression and localization in various types of carcinomas of the thyroid gland

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